View source for 6r70


==Endogeneous native human 20S proteasome==
<SX load='6r70' size='340' side='right' viewer='molstar' caption='[[6r70]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r70]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R70 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r70 OCA], [https://pdbe.org/6r70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r70 RCSB], [https://www.ebi.ac.uk/pdbsum/6r70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r70 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/PSB7_HUMAN PSB7_HUMAN] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity.
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== Publication Abstract from PubMed ==
High-resolution structural information is essential to understand protein function. Protein-structure determination needs a considerable amount of protein, which can be challenging to produce, often involving harsh and lengthy procedures. In contrast, the several thousand to a few million protein particles required for structure determination by cryogenic electron microscopy (cryo-EM) can be provided by miniaturized systems. Here, we present a microfluidic method for the rapid isolation of a target protein and its direct preparation for cryo-EM. Less than 1 muL of cell lysate is required as starting material to solve the atomic structure of the untagged, endogenous human 20S proteasome. Our work paves the way for high-throughput structure determination of proteins from minimal amounts of cell lysate and opens more opportunities for the isolation of sensitive, endogenous protein complexes.

Microfluidic protein isolation and sample preparation for high-resolution cryo-EM.,Schmidli C, Albiez S, Rima L, Righetto R, Mohammed I, Oliva P, Kovacik L, Stahlberg H, Braun T Proc Natl Acad Sci U S A. 2019 Jul 10. pii: 1907214116. doi:, 10.1073/pnas.1907214116. PMID:31292253<ref>PMID:31292253</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6r70" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteasome 3D structures|Proteasome 3D structures]]
== References ==
<references/>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Albiez S]]
[[Category: Braun T]]
[[Category: Kovacik L]]
[[Category: Mohammed I]]
[[Category: Oliva P]]
[[Category: Righetto R]]
[[Category: Rima L]]
[[Category: Schmidli C]]
[[Category: Stahlberg H]]